ID A0A0L8M953_9ACTN Unreviewed; 342 AA. AC A0A0L8M953; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 02-JUN-2021, entry version 29. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627}; DE Short=TDH {ECO:0000256|HAMAP-Rule:MF_00627}; DE EC=1.1.1.103 {ECO:0000256|HAMAP-Rule:MF_00627}; GN Name=tdh {ECO:0000256|HAMAP-Rule:MF_00627, GN ECO:0000313|EMBL:KOG46915.1}; GN ORFNames=ADK74_11460 {ECO:0000313|EMBL:KOG46915.1}; OS Streptomyces decoyicus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG46915.1, ECO:0000313|Proteomes:UP000037606}; RN [1] {ECO:0000313|Proteomes:UP000037606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U., RA Blagden T., Winegar R.A.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- CC amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + CC NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948; CC EC=1.1.1.103; Evidence={ECO:0000256|HAMAP-Rule:MF_00627}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00627}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00627}; CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo- CC reductase pathway; glycine from L-threonine: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KOG46915.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LGUU01000115; KOG46915.1; -; Genomic_DNA. DR RefSeq; WP_030083208.1; NZ_LGUU01000115.1. DR EnsemblBacteria; KOG46915; KOG46915; ADK74_11460. DR PATRIC; fig|249567.6.peg.2470; -. DR UniPathway; UPA00046; UER00505. DR Proteomes; UP000037606; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00627; Thr_dehydrog; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR004627; L-Threonine_3-DHase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00627}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00627}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00627}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00627}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00627}. FT DOMAIN 25..133 FT /note="ADH_N" FT /evidence="ECO:0000259|Pfam:PF08240" FT DOMAIN 174..300 FT /note="ADH_zinc_N" FT /evidence="ECO:0000259|Pfam:PF00107" FT NP_BIND 262..264 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT NP_BIND 286..287 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT ACT_SITE 40 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT ACT_SITE 43 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 38 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 63 FT /note="Zinc 1; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 64 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 93 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 96 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 99 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 107 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 175 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 195 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 200 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT SITE 148 FT /note="Important for catalytic activity for the proton FT relay mechanism but does not participate directly in the FT coordination of zinc atom" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" SQ SEQUENCE 342 AA; 36452 MW; 5EBC59BEF056238A CRC64; MKALVKQKAE PGLWLMDVPE PAVGPGDVLI KVLRTGICGT DLHIRAWDGW AQQAVATPMT IGHEFVGEVV ETGRDVADIK AGDLVSGEGH LVCGKCRNCQ AGRRHLCRAT VGLGVGRDGA FAEYVALPAA NVWVHRVPVD LDIAAVFDPF GNAVHTALSF PLVGEDVLIT GAGPIGIMAA AVARHAGARN VVITDVSEPR LELARKVGVS LALNVAEAKI ADGQRELGLR EGFDIGLEMS GRPEAMRDMI ANMTHGGRIA VLGLPSEQFP VDWSRIVTSM ITIKGIYGRE MFETWYAMSV LLEGGLDLAP VITGRYSHQD FDAAFDDAAS GRSGKIILDW TA //